CAZyme Information: MGYG000002817_05743

Basic Information

• Species: Paenibacillus_B sp900539405
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B sp900539405
• CAZyme ID: MGYG000002817_05743
• CAZy Family: GT51
• CAZyme Description: Monofunctional biosynthetic peptidoglycan transglycosylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
314		35362.65	10.0163

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002817	6425839	MAG	United States	North America

• Gene Location: Start: 7596; End: 8540 Strand: +

Full Sequence      

MRIIRWEHPAKGSLALHSPIRAMRAHQGEWTGSPGGHRASASEQRPVKQDQVQTDTESAS
TPIGRSIAHVWRRWVIYGVTAAILAPVIGWFMMAGLAPAWMDEAKLAALREEIREGVSAD
GRHIVRLKDMPAYVTEALLAIEDHRYRYHPGIDPIGLARSVWINVTKQQKAQGGSTITMQ
LARNLFLTQDKLYSRKFKEMAIAANLEWRYTKDEILEMYLNKVYFGHGKYGIEDAARFYF
GKTAGASDALETINEAEAAMLVGLLKAPERLSPRKHPAAAEHRQNVVLRRMVELGWLTEG
ERQHLKKAEIVHAS

Enzyme Prediction     

No EC number prediction in MGYG000002817_05743.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT51	118	292	3.5e-64	0.9491525423728814

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02074	PBP_1a_fam	1.00e-81	122	312	2	186	penicillin-binding protein, 1A family. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
pfam00912	Transgly	8.25e-81	122	292	13	177	Transglycosylase. The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
COG0744	MrcB	1.50e-78	71	311	7	260	Membrane carboxypeptidase (penicillin-binding protein) [Cell wall/membrane/envelope biogenesis].
COG5009	MrcA	1.58e-69	118	311	53	250	Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis].
TIGR02071	PBP_1b	8.03e-49	101	307	126	330	penicillin-binding protein 1B. Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDM45679.1	9.36e-206	1	314	1	314
SYX81611.1	2.71e-109	45	310	39	307
AYB39777.1	2.14e-70	57	311	6	261
AYK06684.1	2.14e-70	73	310	26	260
ATO50024.1	3.03e-70	57	311	6	261

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3NB6_A	2.97e-42	122	298	20	190	Crystalstructure of Aquifex aeolicus peptidoglycan glycosyltransferase in complex with Methylphosphoryl Neryl Moenomycin [Aquifex aeolicus]
2OQO_A	1.17e-41	122	298	20	190	Crystalstructure of a peptidoglycan glycosyltransferase from a class A PBP: insight into bacterial cell wall synthesis [Aquifex aeolicus VF5],3D3H_A Crystal structure of a complex of the peptidoglycan glycosyltransferase domain from Aquifex aeolicus and neryl moenomycin A [Aquifex aeolicus],3NB7_A Crystal structure of Aquifex Aeolicus Peptidoglycan Glycosyltransferase in complex with Decarboxylated Neryl Moenomycin [Aquifex aeolicus]
5U2G_A	5.63e-36	125	311	43	223	2.6Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20],5U2G_B 2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae [Haemophilus influenzae Rd KW20]
4OON_A	3.36e-35	125	314	42	224	Crystalstructure of PBP1a in complex with compound 17 ((4Z,8S,11E,14S)-5-(2-amino-1,3-thiazol-4-yl)-14-(5,6-dihydroxy-1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-8-formyl-2-methyl-6-oxo-3,10-dioxa-4,7,11-triazatetradeca-4,11-diene-2,12,14-tricarboxylic acid) [Pseudomonas aeruginosa PAO1]
3UDF_A	2.52e-30	125	303	42	214	ChainA, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDF_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDI_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UDX_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE0_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_A Chain A, Penicillin-binding protein 1a [Acinetobacter baumannii],3UE1_B Chain B, Penicillin-binding protein 1a [Acinetobacter baumannii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q07259	3.27e-43	125	301	50	219	Putative transglycosylase H16_A0665 OS=Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) OX=381666 GN=H16_A0665 PE=3 SV=2
P38050	2.09e-39	75	301	13	240	Penicillin-binding protein 1F OS=Bacillus subtilis (strain 168) OX=224308 GN=pbpF PE=2 SV=2
O66874	2.40e-37	122	298	63	233	Penicillin-binding protein 1A OS=Aquifex aeolicus (strain VF5) OX=224324 GN=mrcA PE=1 SV=1
P31776	1.99e-36	125	311	58	238	Penicillin-binding protein 1A OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=mrcA PE=1 SV=2
Q9KNU5	4.84e-36	125	301	69	239	Penicillin-binding protein 1A OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=mrcA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
74	96